The proposed research is directed at a comprehensive spectral, kinetic and thermodynamic investigation of the properties of heme and hemin, intercalated in a variety of systematically chosen micelles, with such nucleophiles as molecular oxygen, carbon monoxide, cyanate and nitrous oxide. The overall objectives are two-fold. First, it is hoped that by studying the properties stated above, a more critical evaluation of the effect of environment on the reactive sites of hemoglobin and other hemoproteins may be obtained by comparison with model systems, with regard to hydrophobicity and structural constraints. Factors responsible for reversibility or oxidation of hemes by molecular oxygen in such micellar environments will be emphasized. Secondly, since cyanate is known to alleviate the symptoms of sickle Cell Anemia, a study will be initiated using the present model systems to investigate heme-cyanate coordinate bonding as a possible important precursor intermediate to the actual carbamylation reaction. The methods to be used in approaching the above problems will be quite diverse. Since many of the reactions are expected to be fast (on the msec or micron sec time scale), these will be investigated by the use of stopped-flow and temperature jump perturbation techniques. To gain insight on the structural constraints imposed by micelles on metalloporphyrins, fluorescence and nuclear magnetic resonance will be used with the metalloporphyrins as fluorescent and paramagnetic probes. Equilibria between the intercalated heme and the above nulceophiles lends itself to investigation by uv and visible spectral differences.